Kowalska M A, Cierniewski C S
Thromb Haemost. 1982 Aug 24;48(1):21-3.
The tryptophan fluorescence of fibrinogen and its final degradation products--fragment D and E--were compared. Fibrinogen and its derivatives exhibit identical emission and excitation spectra. Their fluorescence intensity is influenced to a different extent by pH titration and temperature. Our studies showed that tryptophan residues of core fragments D and E are much more exposed to quenching effects of acrylamide and ions than intact fibrinogen, which may be caused by conformational changes occurring over the domains during plasmin digestion of fibrinogen molecule.
对纤维蛋白原及其最终降解产物——D片段和E片段的色氨酸荧光进行了比较。纤维蛋白原及其衍生物呈现出相同的发射光谱和激发光谱。它们的荧光强度受pH滴定和温度的影响程度不同。我们的研究表明，与完整的纤维蛋白原相比，核心片段D和E中的色氨酸残基更容易受到丙烯酰胺和离子的猝灭作用影响，这可能是由于纤维蛋白原分子在纤溶酶消化过程中结构域发生构象变化所致。
